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Database: UniProt
Entry: A0A0T6AL68_9BACT
LinkDB: A0A0T6AL68_9BACT
Original site: A0A0T6AL68_9BACT 
ID   A0A0T6AL68_9BACT        Unreviewed;       203 AA.
AC   A0A0T6AL68;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Alkyl hydroperoxide reductase/thiol specific antioxidant/Mal allergen {ECO:0000313|EMBL:KRT75839.1};
GN   ORFNames=XU14_C0090G0004 {ECO:0000313|EMBL:KRT75839.1};
OS   Armatimonadetes bacterium CSP1-3.
OC   Bacteria; Armatimonadota.
OX   NCBI_TaxID=1640515 {ECO:0000313|EMBL:KRT75839.1, ECO:0000313|Proteomes:UP000051026};
RN   [1] {ECO:0000313|EMBL:KRT75839.1, ECO:0000313|Proteomes:UP000051026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-3 {ECO:0000313|EMBL:KRT75839.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRT75839.1}.
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DR   EMBL; LDXQ01000090; KRT75839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6AL68; -.
DR   PATRIC; fig|1640515.3.peg.2298; -.
DR   Proteomes; UP000051026; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51318; TAT; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
FT   DOMAIN          56..198
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          37..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   203 AA;  21852 MW;  E89475367CEF8E72 CRC64;
     MSRGRRVLLG ALVGVLIGGA AAYLLFRPVS SPARNPTSLQ PYPLASTPGQ PPARPLQARR
     PAPEFALPSL RGGEIRLSDF RGKVVLLNFF ASWCAPCAAE APDLRATSEK YGGRNVVFVG
     VAILDEFKEA QAFLERHRLP YPAAFDRGNK IMERYQVTGL PTSIFIDPAG MIVSRFVGPF
     IGPEGVAELE RRLAQAGAQP AAP
//
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